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Yorodumi- PDB-9hch: Mouse mitoribosome large subunit assembly intermediate bound to N... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9hch | ||||||||||||||||||||||||||||||
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| Title | Mouse mitoribosome large subunit assembly intermediate bound to NSUN4, METRF4, GTPBP7 and the MALSU1-L0R8F8-mt-ACP complex, State C1 (SAMC knock-out) | ||||||||||||||||||||||||||||||
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Keywords | RIBOSOME / mitochondria / large subunit / assembly intermediate | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationMitochondrial ribosome-associated quality control / Mitochondrial translation elongation / mitochondrial small ribosomal subunit assembly / mRNA (cytidine-5-)-methyltransferase activity / regulation of respiratory system process / regulation of mitochondrial transcription / Mitochondrial translation termination / mitochondrial RNA catabolic process / regulation of mitochondrial translation / negative regulation of mitochondrial translation ...Mitochondrial ribosome-associated quality control / Mitochondrial translation elongation / mitochondrial small ribosomal subunit assembly / mRNA (cytidine-5-)-methyltransferase activity / regulation of respiratory system process / regulation of mitochondrial transcription / Mitochondrial translation termination / mitochondrial RNA catabolic process / regulation of mitochondrial translation / negative regulation of mitochondrial translation / rRNA (cytosine-C5-)-methyltransferase activity / mitochondrial large ribosomal subunit assembly / Protein lipoylation / Mitochondrial Fatty Acid Beta-Oxidation / negative regulation of ribosome biogenesis / Complex I biogenesis / positive regulation of mitochondrial translation / Respiratory electron transport / rRNA import into mitochondrion / ribonuclease III activity / mitochondrial translational termination / mitochondrial translational elongation / mitochondrial ribosome assembly / Mitochondrial protein degradation / translation release factor activity, codon nonspecific / camera-type eye development / mitochondrial fission / iron-sulfur cluster assembly complex / mitochondrial large ribosomal subunit binding / mitochondrial large ribosomal subunit / peptidyl-tRNA hydrolase / translation release factor activity / mitochondrial [2Fe-2S] assembly complex / mitochondrial ribosome / rRNA methylation / mitochondrial small ribosomal subunit / peptidyl-tRNA hydrolase activity / [2Fe-2S] cluster assembly / mitochondrial translation / iron-sulfur cluster assembly / ribosomal large subunit binding / proton motive force-driven mitochondrial ATP synthesis / mitochondrial respiratory chain complex I assembly / respiratory chain complex I / RNA processing / rescue of stalled cytosolic ribosome / cytosolic ribosome / Transferases; Transferring one-carbon groups; Methyltransferases / aerobic respiration / cellular response to leukemia inhibitory factor / ribosomal large subunit biogenesis / mitochondrion organization / fibrillar center / fatty acid biosynthetic process / rRNA processing / cell junction / double-stranded RNA binding / large ribosomal subunit / heart development / 5S rRNA binding / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / mitochondrial inner membrane / negative regulation of translation / rRNA binding / nuclear body / structural constituent of ribosome / ribosome / translation / mitochondrial matrix / ribonucleoprotein complex / protein domain specific binding / nucleotide binding / GTPase activity / mRNA binding / apoptotic process / GTP binding / nucleolus / structural molecule activity / mitochondrion / RNA binding / nucleoplasm / metal ion binding / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.85 Å | ||||||||||||||||||||||||||||||
Authors | Singh, V. / Rorbach, J. / Freyer, C. / Amunts, A. / Wredenberg, A. | ||||||||||||||||||||||||||||||
| Funding support | Sweden, Denmark, 3items
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Citation | Journal: Nat Commun / Year: 2025Title: The mitochondrial methylation potential gates mitoribosome assembly. Authors: Ruth I C Glasgow / Vivek Singh / Lucía Peña-Pérez / Alissa Wilhalm / Marco F Moedas / David Moore / Florian A Rosenberger / Xinping Li / Ilian Atanassov / Mira Saba / Miriam Cipullo / ...Authors: Ruth I C Glasgow / Vivek Singh / Lucía Peña-Pérez / Alissa Wilhalm / Marco F Moedas / David Moore / Florian A Rosenberger / Xinping Li / Ilian Atanassov / Mira Saba / Miriam Cipullo / Joanna Rorbach / Anna Wedell / Christoph Freyer / Alexey Amunts / Anna Wredenberg / ![]() Abstract: S-adenosylmethionine (SAM) is the principal methyl donor in cells and is essential for mitochondrial gene expression, influencing RNA modifications, translation, and ribosome biogenesis. Using direct ...S-adenosylmethionine (SAM) is the principal methyl donor in cells and is essential for mitochondrial gene expression, influencing RNA modifications, translation, and ribosome biogenesis. Using direct long-read RNA sequencing in mouse tissues and embryonic fibroblasts, we show that processing of the mitochondrial ribosomal gene cluster fails in the absence of mitochondrial SAM, leading to an accumulation of unprocessed precursors. Proteomic analysis of ribosome fractions revealed these precursors associated with processing and assembly factors, indicating stalled biogenesis. Structural analysis by cryo-electron microscopy demonstrated that SAM-dependent methylation is required for peptidyl transferase centre formation during mitoribosome assembly. Our findings identify a critical role for SAM in coordinating mitoribosomal RNA processing and large subunit maturation, linking cellular methylation potential to mitochondrial translation capacity. | ||||||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9hch.cif.gz | 4.6 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9hch.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9hch.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hc/9hch ftp://data.pdbj.org/pub/pdb/validation_reports/hc/9hch | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 52049MC ![]() 9e9cC ![]() 9hccC ![]() 9hcdC ![]() 9hceC ![]() 9hcfC ![]() 9hcgC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-RNA chain , 2 types, 2 molecules AB
| #1: RNA chain | Mass: 508601.906 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #2: RNA chain | Mass: 21862.076 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+Large ribosomal subunit protein ... , 50 types, 50 molecules DEFHIJKLMNOPQRSTUVWXYZ0123467b...
-Protein , 4 types, 4 molecules xvwy
| #25: Protein | Mass: 39973.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: Q9CZ57, Transferases; Transferring one-carbon groups; Methyltransferases |
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| #48: Protein | Mass: 8444.846 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #49: Protein | Mass: 17390.289 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #57: Protein | Mass: 40306.180 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Mitochondrial ... , 2 types, 2 molecules uz
| #47: Protein | Mass: 26055.053 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #56: Protein | Mass: 36732.039 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 5 types, 104 molecules 








| #59: Chemical | ChemComp-MG / #60: Chemical | #61: Chemical | ChemComp-FES / | #62: Chemical | ChemComp-GNP / | #63: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Assembly intermediate of the mitoribosome large subunit Type: RIBOSOME Entity ID: #1, #25, #3-#6, #8-#11, #13-#24, #26-#54, #12, #7, #55-#58, #2 Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 400 nm |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.20.1_4487: / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.85 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 55461 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi





Sweden,
Denmark, 3items
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FIELD EMISSION GUN